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dc.contributor.authorWang, Yu-Kuoen_US
dc.contributor.authorHuang, Sheng-Cihen_US
dc.contributor.authorChang, Chin-Yuanen_US
dc.contributor.authorHuang, Wan-Tingen_US
dc.contributor.authorLiao, Man-Junen_US
dc.contributor.authorYip, Bak-Sauen_US
dc.contributor.authorChou, Feng-Paien_US
dc.contributor.authorLi, Thomas Tien-Hsiungen_US
dc.contributor.authorWu, Tung-Kungen_US
dc.date.accessioned2019-08-02T02:15:35Z-
dc.date.available2019-08-02T02:15:35Z-
dc.date.issued2019-07-08en_US
dc.identifier.issn2045-2322en_US
dc.identifier.urihttp://dx.doi.org/10.1038/s41598-019-46354-xen_US
dc.identifier.urihttp://hdl.handle.net/11536/152259-
dc.description.abstractOligomerization of protein into specific quaternary structures plays important biological functions, including regulation of gene expression, enzymes activity, and cell-cell interactions. Here, we report the determination of two crystal structures of the Grimontia hollisae (formally described as Vibrio hollisae) thermostable direct hemolysin (Gh-TDH), a pore-forming toxin. The toxin crystalized in the same space group of P2(1)2(1)2, but with two different crystal packing patterns, each revealing three consistent tetrameric oligomerization forms called Oligomer-I, -II, and -III. A central pore with comparable depth of similar to 50 angstrom but differing in shape and size was observed in all determined toxin tetrameric oligomers. A common motif of a toxin dimer was found in all determined structures, suggesting a plausible minimum functional unit within the tetrameric structure in cell membrane binding and possible hemolytic activity. Our results show that bacterial toxins may form a single or highly symmetric oligomerization state when exerting their biological functions. The dynamic nature of multiple symmetric oligomers formed upon release of the toxin may open a niche for bacteria survival in harsh living environments.en_US
dc.language.isoen_USen_US
dc.titleMultiple Pleomorphic Tetramers of Thermostable Direct Hemolysin from Grimontia hollisae in Exerting Hemolysis and Membrane Bindingen_US
dc.typeArticleen_US
dc.identifier.doi10.1038/s41598-019-46354-xen_US
dc.identifier.journalSCIENTIFIC REPORTSen_US
dc.citation.volume9en_US
dc.citation.spage0en_US
dc.citation.epage0en_US
dc.contributor.department交大名義發表zh_TW
dc.contributor.department生物科技學系zh_TW
dc.contributor.departmentNational Chiao Tung Universityen_US
dc.contributor.departmentDepartment of Biological Science and Technologyen_US
dc.identifier.wosnumberWOS:000474335800030en_US
dc.citation.woscount0en_US
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